X-ray diffraction
2.5Å resolution

Crystal structure of CTR1 kinase domain mutant D676N in complex with staurosporine

Source organism: Arabidopsis thaliana
Entry authors: Mayerhofer H, Panneerselvam S, Mueller-Dieckmann J

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Serine/threonine-protein kinase CTR1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 309 amino acids
Theoretical weight: 35.22 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
  • Canonical: Q05609 (Residues: 540-821; Coverage: 34%)
Gene names: At5g03730, CTR1, F17C15_150
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P42212
Unit cell:
a: 122.334Å b: 122.334Å c: 95.011Å
α: 90° β: 90° γ: 90°
R R work R free
0.197 0.195 0.232
Expression system: Escherichia coli